Cell
MinireviewTranscriptional regulation by dimerization: Two sides to an incestuous relationship
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Cited by (294)
Transcriptome analysis reveals gene expression changes of the basidiomycetous yeast Apiotrichum mycotoxinivorans in response to ochratoxin A exposure
2022, Ecotoxicology and Environmental SafetyCitation Excerpt :Most ATPs generated during aerobic glucose catabolism are derived from this electron transport chain process (Schertl and Braun, 2014), indicating increased ATP production. Additionally, enriched protein heterodimerization activity (GO:0046982) can enhance the regulatory potential of transcription, transporters, and enzymes (Jones, 1990). From this perspective, we deduced that OTA exposure may suppress replication and transcription, increase aerobic respiration and ATP production, cause ribosomal stress, and promote protein transport.
Conformational stability and folding mechanisms of dimeric proteins
2008, Progress in Biophysics and Molecular BiologyCitation Excerpt :Formation of the dimers is controlled by transcriptional/translational control and degradation. An unstable monomer may be important to facilitate rapid turning off of signaling (Jones, 1990). In recent years, protein misfolding has been implicated in a vast and expanding array of diverse diseases, including many neurodegenerative diseases, such as Alzheimer's, Huntington's, Creutzfeld-Jakob, and amyotrophic lateral sclerosis, as well as cancer, and cystic fibrosis (for reviews see (Gregersen, 2006; Ross and Poirier, 2004; Stefani and Dobson, 2003)).
Dimerization of BTas is required for the transactivational activity of bovine foamy virus
2008, VirologyCitation Excerpt :Many eukaryotic transcription factors take the form of dimers or higher-order multimers as an absolute requirement for biological activity (Bogerd et al., 1993; Chen et al., 1992; Hu et al., 1990; Landschulz et al., 1988; McIntyre et al., 1993; Williams and Tjian, 1991; Xia and Lai, 1992; Zapp et al., 1991). Structural domains or motifs mediating specific interactions have been characterized, such as the leucine zipper, helix–loop–helix, and helix–span–helix proteins (Jones, 1990; Lamb and McKnight, 1991; Landschulz et al., 1988). In addition, several proteins, such as E7, Tat and Rex, possess only one dimerization domain (Bogerd and Greene, 1993; Frankel et al., 1988; McIntyre et al., 1993).
1α, 25(OH)<inf>2</inf>Vitamin D<inf>3</inf>Vitamin D Nuclear Receptor (VDR) and Plasma Vitamin D-Binding Protein (DBP) Structures and Ligand Shape Preferences for Genomic and Rapid Biological Responses
2008, Principles of Bone Biology: Volume 1-2, Third EditionTranscriptional repression of human immunodeficiency virus type 1 by AP-4
2006, Journal of Biological ChemistryCitation Excerpt :There are a number of transcription factors acting as repressors. However, the mechanisms of their actions are not uniform and multiple modes of action are reported including: 1) inhibition of transcriptional activators upon its DNA binding or interaction with co-activators (36-38), 2) prevention of the binding of general transcription factors such as TBP (TFIID) and TFIIB to the promoter (39-43), 3) direct repression of promoter activity by recruiting co-repressors (8, 28, 30), 4) alteration of chromatin structure (19, 40), and 5) inhibition of transcriptional elongation (44, 45). AP-4 appears to exert transcriptional repression of HIV-1 promoter through bimodal mechanisms: 1) masking the HIV-1 TATA element from TBP binding and 2) recruiting HDAC1.